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O34522 (TRMB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA (guanine-N(7)-)-methyltransferase

EC=2.1.1.33
Alternative name(s):
BsTrmB
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase
Gene names
Name:trmB
Synonyms:ytmQ
Ordered Locus Names:BSU29900
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. HAMAP-Rule MF_01057

Catalytic activity

S-adenosyl-L-methionine + guanine46 in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine46 in tRNA. Ref.3

Pathway

tRNA modification; N(7)-methylguanine-tRNA biosynthesis. HAMAP-Rule MF_01057

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.

Ontologies

Keywords
   Biological processtRNA processing
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functiontRNA (guanine-N7-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_0000171295

Regions

Region124 – 1296Interaction with RNA Potential
Region191 – 1944Substrate binding By similarity

Sites

Active site1181 By similarity
Binding site441S-adenosyl-L-methionine By similarity
Binding site691S-adenosyl-L-methionine By similarity
Binding site961S-adenosyl-L-methionine By similarity
Binding site1181S-adenosyl-L-methionine By similarity
Binding site1221Substrate By similarity
Binding site1541Substrate By similarity

Secondary structure

....................................... 213
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O34522 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 28C34F163EB2DD69

FASTA21324,504
        10         20         30         40         50         60 
MRMRHKPWAD DFLAENADIA ISNPADYKGK WNTVFGNDNP IHIEVGTGKG QFISGMAKQN 

        70         80         90        100        110        120 
PDINYIGIEL FKSVIVTAVQ KVKDSEAQNV KLLNIDADTL TDVFEPGEVK RVYLNFSDPW 

       130        140        150        160        170        180 
PKKRHEKRRL TYSHFLKKYE EVMGKGGSIH FKTDNRGLFE YSLKSFSEYG LLLTYVSLDL 

       190        200        210 
HNSNLEGNIM TEYEEKFSAL GQPIYRAEVE WRT 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46) methyltransferase."
Zegers I., Gigot D., van Vliet F., Tricot C., Aymerich S., Bujnicki J.M., Kosinski J., Droogmans L.
Nucleic Acids Res. 34:1925-1934(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), CATALYTIC ACTIVITY.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF008220 Genomic DNA. Translation: AAC00285.1.
AL009126 Genomic DNA. Translation: CAB14968.1.
PIRB69997.
RefSeqNP_390868.1. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FCAX-ray2.10A/B1-213[»]
ProteinModelPortalO34522.
SMRO34522. Positions 10-213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU29900.

Proteomic databases

PaxDbO34522.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14968; CAB14968; BSU29900.
GeneID936447.
KEGGbsu:BSU29900.
PATRIC18977886. VBIBacSub10457_3131.

Organism-specific databases

GenoListBSU29900. [Micado]

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000251689.
KOK03439.
OMADNVMTEY.
OrthoDBEOG6K6VBC.
PhylomeDBO34522.

Enzyme and pathway databases

BioCycBSUB:BSU29900-MONOMER.
UniPathwayUPA00989.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
HAMAPMF_01057. tRNA_methyltr_TrmB.
InterProIPR029063. SAM-dependent_MTases-like.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
PfamPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
TIGRFAMsTIGR00091. TIGR00091. 1 hit.
PROSITEPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO34522.

Entry information

Entry nameTRMB_BACSU
AccessionPrimary (citable) accession number: O34522
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList